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  1. Article ; Online: Helical reconstruction, again.

    Egelman, Edward H

    Current opinion in structural biology

    2024  Volume 85, Page(s) 102788

    Abstract: Many protein and nucleoprotein complexes exist as helical polymers. As a result, much effort has been invested in developing methods for using electron microscopy to determine the structure of these assemblies. With the revolution in cryo-electron ... ...

    Abstract Many protein and nucleoprotein complexes exist as helical polymers. As a result, much effort has been invested in developing methods for using electron microscopy to determine the structure of these assemblies. With the revolution in cryo-electron microscopy (cryo-EM), it has now become routine to reach a near-atomic level of resolution for these structures, and it is the exception when this is not possible. However, the greatest challenge is frequently determining the correct symmetry. This review focuses on why this can be so difficult and the current absence of a better approach than trial-and-error.
    MeSH term(s) Cryoelectron Microscopy/methods ; Microscopy, Electron
    Language English
    Publishing date 2024-02-23
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2024.102788
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  2. Article ; Online: Mutate or die: Atomic structures explain bacterial SOS induction.

    Egelman, Edward H

    Proceedings of the National Academy of Sciences of the United States of America

    2023  Volume 120, Issue 5, Page(s) e2221605120

    MeSH term(s) SOS Response, Genetics ; DNA Repair ; Bacteria ; Bacterial Proteins/genetics ; Genes, Bacterial
    Chemical Substances Bacterial Proteins
    Language English
    Publishing date 2023-01-24
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Comment
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2221605120
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  3. Article ; Online: Cryo-EM: Ice Is Nice, but Good Ice Can Be Hard to Find.

    Egelman, Edward H

    Biophysical journal

    2020  Volume 118, Issue 6, Page(s) 1238–1239

    MeSH term(s) Cryoelectron Microscopy ; Ice
    Chemical Substances Ice
    Language English
    Publishing date 2020-02-01
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2020.01.026
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    Zs.A 235: Show issues Location:
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  4. Article ; Online: Hooked on motility.

    Egelman, Edward H

    Nature structural & molecular biology

    2019  Volume 26, Issue 10, Page(s) 848–849

    MeSH term(s) Bacteria/cytology ; Bacteria/ultrastructure ; Bacterial Proteins/ultrastructure ; Cryoelectron Microscopy ; Flagella/ultrastructure ; Models, Molecular ; Molecular Motor Proteins/ultrastructure ; Salmonella typhimurium/cytology ; Salmonella typhimurium/ultrastructure
    Chemical Substances Bacterial Proteins ; Molecular Motor Proteins
    Language English
    Publishing date 2019-09-30
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-019-0302-2
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    Zs.MG 56: Show issues

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  5. Article ; Online: Cryo-EM structure of flagellotropic bacteriophage Chi.

    Sonani, Ravi R / Esteves, Nathaniel C / Scharf, Birgit E / Egelman, Edward H

    Structure (London, England : 1993)

    2024  

    Abstract: The flagellotropic bacteriophage χ (Chi) infects bacteria via the flagellar filament. Despite years of study, its structural architecture remains partly characterized. Through cryo-EM, we unveil χ's nearly complete structure, encompassing capsid, neck, ... ...

    Abstract The flagellotropic bacteriophage χ (Chi) infects bacteria via the flagellar filament. Despite years of study, its structural architecture remains partly characterized. Through cryo-EM, we unveil χ's nearly complete structure, encompassing capsid, neck, tail, and tail tip. While the capsid and tail resemble phage YSD1, the neck and tail tip reveal new proteins and their arrangement. The neck shows a unique conformation of the tail tube protein, forming a socket-like structure for attachment to the neck. The tail tip comprises four proteins, including distal tail protein (DTP), two baseplate hub proteins (BH1P and BH2P), and tail tip assembly protein (TAP) exhibiting minimal organization compared to other siphophages. Deviating from the consensus in other siphophages, DTP in χ forms a trimeric assembly, reducing tail symmetry from 6-fold to 3-fold at the tip. These findings illuminate the previously unexplored structural organization of χ's neck and tail tip.
    Language English
    Publishing date 2024-04-03
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2024.03.011
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  6. Article ; Online: Stabilization of F-actin by Salmonella effector SipA resembles the structural effects of inorganic phosphate and phalloidin.

    Niedzialkowska, Ewa / Runyan, Lucas A / Kudryashova, Elena / Egelman, Edward H / Kudryashov, Dmitri S

    Structure (London, England : 1993)

    2024  

    Abstract: Entry of Salmonella into host enterocytes relies on its pathogenicity island 1 effector SipA. We found that SipA binds to F-actin in a 1:2 stoichiometry with sub-nanomolar affinity. A cryo-EM reconstruction revealed that SipA's globular core binds at the ...

    Abstract Entry of Salmonella into host enterocytes relies on its pathogenicity island 1 effector SipA. We found that SipA binds to F-actin in a 1:2 stoichiometry with sub-nanomolar affinity. A cryo-EM reconstruction revealed that SipA's globular core binds at the groove between actin strands, whereas the extended C-terminal arm penetrates deeply into the inter-strand space, stabilizing F-actin from within. The unusually strong binding of SipA is achieved by a combination of fast association via the core and very slow dissociation dictated by the arm. Similar to P
    Language English
    Publishing date 2024-03-19
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2024.02.022
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  7. Article ; Online: Cryo-EM is a powerful tool, but helical applications can have pitfalls.

    Egelman, Edward H / Wang, Fengbin

    Soft matter

    2021  Volume 17, Issue 12, Page(s) 3291–3293

    Abstract: In structural biology, cryo-electron microscopy (cryo-EM) has emerged as the main technique for determining the atomic structures of macromolecular complexes. This has largely been due to the introduction of direct electron detectors, which have allowed ... ...

    Abstract In structural biology, cryo-electron microscopy (cryo-EM) has emerged as the main technique for determining the atomic structures of macromolecular complexes. This has largely been due to the introduction of direct electron detectors, which have allowed for routinely reaching a near-atomic resolution when imaging such complexes. In chemistry and materials science, the applications of cryo-EM have been much more limited. A recent paper (Z. Li et al., Chemically Controlled Helical Polymorphism In Protein Tubes By Selective Modulation Of Supramolecular Interactions, J. Am. Chem. Soc. 2019, 141, 19448-19457) has used low resolution cryo-EM to analyze polymorphic helical tubes formed by a tetrameric protein, and has made detailed models for the interfaces between the tetramers in these assemblies. Due to intrinsic ambiguities in determining the correct helical symmetry, we show that many of the models are likely to be wrong. This note highlights both the enormous potential for using cryo-EM, and also the pitfalls possible for helical assemblies when a near-atomic level of resolution is not reached.
    Language English
    Publishing date 2021-03-17
    Publishing country England
    Document type Journal Article
    ZDB-ID 2191476-X
    ISSN 1744-6848 ; 1744-683X
    ISSN (online) 1744-6848
    ISSN 1744-683X
    DOI 10.1039/d1sm00282a
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  8. Article: Stabilization of F-actin by

    Niedzialkowska, Ewa / Runyan, Lucas A / Kudryashova, Elena / Egelman, Edward H / Kudryashov, Dmitri S

    bioRxiv : the preprint server for biology

    2023  

    Abstract: ... Entry ... ...

    Abstract Entry of
    Language English
    Publishing date 2023-12-26
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.12.26.573373
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  9. Article ; Online: Models are useful until high-resolution structures are available.

    Wang, Fengbin / Craig, Lisa / Liu, Xing / Rensing, Christopher / Egelman, Edward H

    Trends in microbiology

    2023  Volume 31, Issue 6, Page(s) 550–551

    MeSH term(s) Protein Conformation ; Models, Molecular
    Language English
    Publishing date 2023-03-31
    Publishing country England
    Document type Letter ; Research Support, N.I.H., Extramural
    ZDB-ID 1158963-2
    ISSN 1878-4380 ; 0966-842X
    ISSN (online) 1878-4380
    ISSN 0966-842X
    DOI 10.1016/j.tim.2023.03.007
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    Zs.A 3738: Show issues Location:
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  10. Article ; Online: Cryo-EM of bacterial pili and archaeal flagellar filaments.

    Egelman, Edward H

    Current opinion in structural biology

    2017  Volume 46, Page(s) 31–37

    Abstract: Recent advances in cryo-electron microscopy (cryo-EM) have opened up the possibility that a large class of biological structures, helical polymers, may now be readily reconstructed at near-atomic resolution. This will have a huge impact, since most of ... ...

    Abstract Recent advances in cryo-electron microscopy (cryo-EM) have opened up the possibility that a large class of biological structures, helical polymers, may now be readily reconstructed at near-atomic resolution. This will have a huge impact, since most of these structures are unlikely to be crystallized. This review focuses on new cryo-EM studies involving three classes of bacterial pili (chaperone-usher, mating, and Type IV) as well as on archaeal flagellar filaments. While it has long been known that one domain within archaeal flagellar filaments is homologous to a domain within bacterial Type IV pilins, the new studies shed light on how homologous and even highly conserved subunits can pack together in different ways with only small changes in sequence.
    MeSH term(s) Archaea/cytology ; Cryoelectron Microscopy/methods ; Fimbriae, Bacterial/metabolism ; Flagella/metabolism
    Language English
    Publishing date 2017-06-10
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2017.05.012
    Database MEDical Literature Analysis and Retrieval System OnLINE

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